Pyrophosphate dependent phosphofructokinase

From Wikipedia, the free encyclopedia

Pyrophosphate: D-Fructose-6-phosphate 1-phosphotransferase
Bacillus stearothermophilus phosphofructokinase
Other names:	PFP, PPi-PFK, pyrophosphate dependent phosphofructokinase
Protein Structure/Function
Molecular Weight:	α-subunit: 66000 (Da) β-subunit: 60000 (Da)
Functions:	Glycolytic/gluconeogenic
Other
Subcellular localization:	Cytosol
Pathway(s):	Glycolysis/Gluconeogenesis
Enzymatic Data
Catalytic activity:	Fructose-6-phosphate + PPi ←→ Fructose-1,6-bisphosphate + Pi
Cofactor(s):	Mg2+
Enzyme Regulation:	Substrates/Products Fructose-2,6-bisphosphate
Database Links
EC number:	2.7.1.90

Pyrophosphate: D-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90, PFP) is an exclusively cytosolic enzyme that catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate in the glycolytic direction, and the de-phosphorylation of fructose-1,6-bisphoshate to fructose-6-phosphate in the gluconeogenic reaction. Reeves et al. (1974) first isolated PFP from Entamoeba histolytica, a lower eukaryote. The first plant PFP isolated was from the leaves of pineapples by Carnal and Black (1979) and it has since been isolated from a variety of plant species and tissues (Stitt 1990).

[edit] References

• Carnal NW, Black CC. (1979) Pyrophosphate-dependent 6-phosphofructokinase, a new glycolytic enzyme in pineapple leaves. Biochemical and biophysical research communications 86:20-26.
• Reeves RE, South DJ, Blytt HT, Warren LG. (1974) Pyrophosphate: D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase. Journal of Biological Chemistry 249:7737-7741. PDF/Abstract
• Stitt M. (1990) Fructose-2,6-bisphosphate as a regulatory molecule in plants. Annual Review of Plant Physiology and Plant Molecular Biology 41:153-185. PDF/Abstract